ID A0A0D3AYP5_BRAOL Unreviewed; 610 AA.
AC A0A0D3AYP5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Amidase domain-containing protein {ECO:0000259|Pfam:PF01425};
GN Name=106325299 {ECO:0000313|EnsemblPlants:Bo2g166250.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo2g166250.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo2g166250.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo2g166250.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
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DR RefSeq; XP_013618795.1; XM_013763341.1.
DR RefSeq; XP_013618796.1; XM_013763342.1.
DR AlphaFoldDB; A0A0D3AYP5; -.
DR STRING; 109376.A0A0D3AYP5; -.
DR EnsemblPlants; Bo2g166250.1; Bo2g166250.1; Bo2g166250.
DR GeneID; 106325299; -.
DR Gramene; Bo2g166250.1; Bo2g166250.1; Bo2g166250.
DR KEGG; boe:106325299; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_0_2_1; -.
DR OMA; TLINMID; -.
DR OrthoDB; 5902at2759; -.
DR Proteomes; UP000032141; Chromosome C2.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProt.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895:SF156; FATTY ACID AMIDE HYDROLASE; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 170..581
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 66304 MW; 5AD731EDFEECC1E9 CRC64;
MGKFKVMKPV NEVDVSCVKY KEEDIKAPHL TGFLFKLFVK MLEAPLIGSL IVESLKKNNG
MTQIFRNTVI PEEPMFRPVF PSQKPELDVV PVGEDESPVN RLETALKCLP QYDPSLSFQA
DSGSSFRYWK IRDYAYAYRS KLTTPSVVAE QIISIIEEFK YDKSPTPFLI SFDANEVRKQ
AEASTHRFEQ GHPISILDGV FITIKDDIDC LPHTTTGGTT WLHEERYVEK DSVVVSRLRS
CGAILLGKAN MHELGMGTSG NNSNYGTTRN PHSPERYTGG SSSGSAAIVA SGLCPAALGT
DGGGSVRIPA SLCGVTGLKT TYGRTDMTGS LCAGGTVEVV SPLASSLEDT LLVYAVILGS
SSADRLNLNP TPPCLPKLLS HNGGNAIGSL RLGKYTTWFN DVHSSDISDK CEDILKLLSN
NHGCQVVEIV VPELEEMRAA HVVSIGSATL CSLTPYCEDG KTPKLSYDTR TSFAIFKSFS
ASDYIAAQCL RRRLMEYHMD IFKNVDVIVT PTCGMTAPLI PPEAVKNGET NFQVAAYLMR
FVVAANLLGF PAISVPVGYD KGGMPIGLQI MGRPWAEATV LTLAAAVEEL APITKKPAVF
HDVLSTKRIH
//